[HTML][HTML] NADPH oxidase activity is independent of p47phox in vitro
JL Freeman, JD Lambeth - Journal of Biological Chemistry, 1996 - ASBMB
The neutrophil superoxide generating NADPH oxidase is activated by the assembly of
cytosolic protein components with a membrane-associated flavocytochrome. The activity can
be reconstituted in vitro using purified cytosolic factors p47 phox, p67 phox, and Rac plus
the phospholipid-reconstituted flavocytochrome b 558. Here, we demonstrate that activity is
reconstituted in the absence of p47 phox when high concentrations of p67 phox and Rac are
used. V max values were the same in the presence or absence of p47 phox, yet p47 phox …
cytosolic protein components with a membrane-associated flavocytochrome. The activity can
be reconstituted in vitro using purified cytosolic factors p47 phox, p67 phox, and Rac plus
the phospholipid-reconstituted flavocytochrome b 558. Here, we demonstrate that activity is
reconstituted in the absence of p47 phox when high concentrations of p67 phox and Rac are
used. V max values were the same in the presence or absence of p47 phox, yet p47 phox …